Skip to main content
SpringerLink
Log in

Transmembrane signalling and paf-acether biosynthesis

  • PAF and Signal Transduction
  • Review
  • Published:
Lipids

Abstract

Expression of lyso paf-acether (lyso paf):acetyl-CoA acetyltransferase and its activation above basal levels by specific agonists controls the rate of paf biosynthesis in proinflammatory cells. Acetyltransferase activation in these cells is due to the rapid postranslational modification of an inactive precursor by phosphorylation, most probably catalyzed by a cAMP-dependent kinase. However, the possibility exists that a calcium/calmodulin-dependent kinase can be implicated as well. Unlike murine cultured mast cells, human neutrophils form paf when stimulated with phorbol myristate acetate (PMA) or diacylglycerol. In both cell types, acetyltransferase is activated by PMA. Controversy exists as to whether PMA activates the remodeling pathway,i.e. the activation of phospholipase A2 and acetyltransferase, or thede novo route through CDPcholine cholinephosphotransferase action on alkylacetylglycerol. There is some indication that PKC might regulate paf biosynthesis. The implication of a GTP-regulated protein has also been postulated in signal transduction leading to paf formation in endothelial cells, neutrophils, and mast cells. The topography of paf formation is discussed in light of the subcellular distribution of acetyltransferase in neutrophils and Krebs II cells.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

GPC:

glycerophosphocholine

G protein:

GTP-regulated protein

IP3 :

inositol 1,4,5-triphosphate

IP4 :

inositol 1,3,4,5-tetraphosphate

lyso paf:

lyso paf-acether, 1-O-alkyl-sn-glycero-3-phosphocholine

paf:

paf-acether, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine

PKA:

cAMP-dependent protein kinase

PKC:

protein kinase C

PLA2 :

phospholipase A2

PLC:

phospholipase C

PMA:

phorbol myristate acetate

References

  1. Ninio, E. (1987) inNew Horizons in Platelet Activating Factor Research (Winslow, C.M., and Lee, M.L., eds.), pp. 27–35, John Wiley and Sons Ltd., Chichester.

    Google Scholar 

  2. Joly, F., Bessou, G., Benveniste, J., and Ninio, E. (1987)Eur. J. Pharmacol. 144, 133–139.

    Article  PubMed  CAS  Google Scholar 

  3. Benhamou, M., Ninio, E., Salem, P., Hiéblot, C., Bessou, G., Pitton, C., Liu, F.T., and Mencia-Huerta, J.M. (1986)J. Immunol. 136, 1385–1392.

    PubMed  CAS  Google Scholar 

  4. Ninio, E., Mencia-Huerta, J.M., and Benveniste, J. (1983)Biochim. Biophys. Acta 751, 298–304.

    PubMed  CAS  Google Scholar 

  5. Ninio, E., Joly, F., and Bessou, G. (1988)Biochim. Biophys. Acta 963, 288–294.

    PubMed  CAS  Google Scholar 

  6. Lenihan, T.J., and Lee, T.-c. (1984)Biochem. Biophys. Res. Commun. 120, 834–839.

    Article  PubMed  CAS  Google Scholar 

  7. Gomez-Cambronero, J., Mato, J.M., Vivanco, F., and Sanchez-Crespo, M. (1987)Biochem. J. 246, 893–898.

    Google Scholar 

  8. Domenech, C., Machado-De Domenech, E., and Söling, H.D. (1987)J. Biol. Chem. 262, 5671–5676.

    PubMed  CAS  Google Scholar 

  9. Ninio, E., Joly, F., Hiéblot, C., Bessou, G., Mencia-Huerta, J.M., and Benveniste, J. (1987)J. Immunol. 139, 154–160.

    PubMed  CAS  Google Scholar 

  10. Albert, D.H., and Snyder, F. (1983)J. Biol. Chem. 258, 97–102.

    PubMed  CAS  Google Scholar 

  11. Sisson, J.H., Prescott, S., McIntyre, T.M., and Zimmerman, G.A. (1987)J. Immunol. 138, 3918–3926.

    PubMed  CAS  Google Scholar 

  12. Leyravaud, S., Bossant, M.J., Joly, F., Benveniste, J., and Ninio, E. (1989)J. Immunol. 143, 245–249.

    PubMed  CAS  Google Scholar 

  13. Hannun, I.A., Loomis, C.R., Merrill, A.H., and Bell, R.M. (1986)J. Biol. Chem. 261, 12604–12609.

    PubMed  CAS  Google Scholar 

  14. McIntyre, T.M., Reinhold, S.L., Prescott, S.M., and Zimmerman, G.A. (1987)J. Biol. Chem. 262, 15370–15376.

    PubMed  CAS  Google Scholar 

  15. Bossant, M.-J., Ninio, E., Delautier, D., and Benveniste, J. (1990)Methods Enzymol. 187, 125–130.

    PubMed  CAS  Google Scholar 

  16. Nieto, M.L., Velasco, S., and Sanchez-Crespo, M. (1988)J. Biol. Chem. 263, 2217–2222.

    PubMed  CAS  Google Scholar 

  17. Gelas, P., Ribbes, G., Record, M., Tercé, F., and Chap, H. (1989)FEBS Lett. 251, 213–218.

    Article  PubMed  CAS  Google Scholar 

  18. Lee, T.-C., Malone, B., and Snyder, F. (1986)J. Biol. Chem. 261, 5373–5377.

    PubMed  CAS  Google Scholar 

  19. Ninio, E., Breton, M., Bidault, J., and Colard, O. (1991)FEBS Lett. 289, 138–140.

    Article  PubMed  CAS  Google Scholar 

  20. Joly, F., Vilgrain, I., Bossant, M.J., Bessou, G., Benveniste, J., and Ninio, E. (1990)Biochem. J. 271, 501–507.

    PubMed  CAS  Google Scholar 

  21. Nishizuka, Y. (1988)Nature 334, 661–665.

    Article  PubMed  CAS  Google Scholar 

  22. Graff, G.M., Young, T.N., Johnson, J.D., and Blackshear, P.J. (1989)J. Biol. Chem. 264, 21818–21823.

    PubMed  CAS  Google Scholar 

  23. Thelen, M., Rosen, A., Nairn, A.C., and Aderem, A. (1991)Nature 351, 320–322.

    Article  PubMed  CAS  Google Scholar 

  24. Yoshimasa, T., Sibley, D.R., Bouvier, M., Lefkowitz, R.J., and Caron, M.G. (1987)Nature 327, 67–70.

    Article  PubMed  CAS  Google Scholar 

  25. Ishizaka, T., Sterk, A.R., Daëron, M., Becker, E.L., and Ishizaka, K. (1985)J. Immunol. 135, 492–501.

    PubMed  CAS  Google Scholar 

  26. Siraganian, R.P. (1988) inInflammation: Basic Principles and Clinical Correlates (Gallin, J.I., Goldstein, I.M., and Snyderman, R., eds.), pp. 513–542, Raven Press, New York.

    Google Scholar 

  27. Mencia-Huerta, J.-M., and Benveniste, J. (1979)Eur. J. Immunol. 9, 409–415.

    PubMed  CAS  Google Scholar 

  28. Bussolino, F., and Benveniste, J. (1980)Immunology 40, 367–376.

    PubMed  CAS  Google Scholar 

  29. Undem, B.J., Torphy, T.J., Goldman, D., and Chilton, F.H. (1990)J. Biol. Chem. 265, 6750–6758.

    PubMed  CAS  Google Scholar 

  30. Garcia, M. del C., Fernandez-Gallardo, S., Gijon, M.A., Garcia, C., Nieto, M.L., and Sanchez-Crespo, M. (1990)Biochem. J. 268, 91–98.

    PubMed  CAS  Google Scholar 

  31. Winslow, C.M., Lewis, R.A., and Austin, K.F. (1981)J. Exp. Med. 154, 1125–1133.

    Article  PubMed  CAS  Google Scholar 

  32. Narisimhan, V., Holowka, D., Fewtrell, C., and Baird, B. (1988)J. Biol. Chem. 263, 19626–19632.

    Google Scholar 

  33. Gomez-Cambronero, J., Durstin, M., Molski, T.F.P., Naccache, P.H., and Sha'afi, R.I. (1989)J. Biol. Chem. 264, 21699–21704.

    CAS  Google Scholar 

  34. Whatley, R.E., Fennell, D.F., Kurrus, J.A., Zimmerman, G.A., McIntyre, T.M., and Prescott, S.M. (1990)J. Biol. Chem. 265, 15550–15559.

    PubMed  CAS  Google Scholar 

  35. Irvine, R.F. (1982)Biochem. J. 204, 3–16.

    PubMed  CAS  Google Scholar 

  36. Chilton, F.H., Ellis, J.M., Olson, S.C., and Wykle, R.L. (1984)J. Biol. Chem. 259, 12014–12019.

    PubMed  CAS  Google Scholar 

  37. Ramesha, C.S., and Pickett, W.C. (1986)J. Biol. Chem. 261, 7592–7595.

    PubMed  CAS  Google Scholar 

  38. Suga, K., Kawasaki, T., Blank, M.L., and Snyder, F. (1990)J. Biol. Chem. 265, 12363–12371.

    PubMed  CAS  Google Scholar 

  39. Seilhamer, J.J., Pruzansky, W., Vadas, P., Plant, S., Miller, J.A., Kloss, J., and Johnson, L.K. (1989)J. Biol. Chem. 264, 5335–5338.

    PubMed  CAS  Google Scholar 

  40. Clark, J.D., Milona, N., and Knopf, J.L. (1990)Proc. Natl. Acad. Sci. USA 87, 7708–7712.

    Article  PubMed  CAS  Google Scholar 

  41. Kramer, R.M., Hessio, C., Johansen, B., Hayes, G., McGray, P., Chow, E.P., Tizard, R., and Pepinsky, R.B. (1989)J. Biol. Chem. 264, 5768–5775.

    PubMed  CAS  Google Scholar 

  42. Kramer, R.M., Patton, G.M., Pritzker, C.R., and Deykin, D. (1984)J. Biol. Chem. 258, 13316–13320.

    Google Scholar 

  43. Robinson, M., Blank, M.L., and Snyder, F. (1985)J. Biol. Chem. 260, 7889–7895.

    PubMed  CAS  Google Scholar 

  44. Sugiura, T., and Waku, K. (1985)Biochem. Biophys. Res. Commun. 127, 384–390.

    Article  PubMed  CAS  Google Scholar 

  45. Colard, O., Breton, M., Pepin, D., Chevy, F., Béréziat, G., and Polonovsky, J. (1989)Biochem. J. 259, 333–339.

    PubMed  CAS  Google Scholar 

  46. Tessner, T.G., Greene, D.G., and Wykle, R.L. (1990)J. Biol. Chem. 265, 21032–21038.

    PubMed  CAS  Google Scholar 

  47. Venable, M.E., Nieto, M.L., Schmitt, J.D., and Wykle, R.L. (1991)J. Biol. Chem. 266, 18691–18698.

    PubMed  CAS  Google Scholar 

  48. Casey, P.J., and Gilman, G.G. (1988)J. Biol. Chem. 263, 2577–2580.

    PubMed  CAS  Google Scholar 

  49. Ribbes, G., Ninio, E., Fontan, P., Record, M., Chap, H., Benveniste, J., and Douste-Blazy, L. (1985)FEBS Lett. 191, 195–199.

    Article  PubMed  CAS  Google Scholar 

  50. Mollinedo, F., Gomez-Cambronero, J., Cano, E., and Sanchez-Crespo, M. (1988)Biochem. Biophys. Res. Commun. 154, 1232–1339.

    Article  PubMed  CAS  Google Scholar 

  51. Record, M., Ribbes, G., Tercé, F., and Chap, H. (1989)J. Cell. Biol. 40, 353–359.

    CAS  Google Scholar 

  52. Radominska-Pyrek, A., Strosznajder, J., Dabrowiecki, Z., Goracci, G., Chojnacki, T., and Horrocks, L.A. (1977)J. Lipid Res. 18, 53–58.

    PubMed  CAS  Google Scholar 

  53. Hardeman, D., and van den Bosch, H. (1989)Biochim. Biophys. Acta 1006, 1–8.

    PubMed  CAS  Google Scholar 

  54. Parker, J., Daniel, L.W., and Walte, M. (1987)J. Biol. Chem. 262, 5385–5393.

    PubMed  CAS  Google Scholar 

  55. Weiss, B.A., and Insel, P.A. (1991)J. Biol. Chem. 266, 2126–2133.

    PubMed  CAS  Google Scholar 

  56. Leslie, C.C., and Channon, J.Y. (1990)Biochim. Biophys. Acta 1045, 261–270.

    PubMed  CAS  Google Scholar 

  57. Dawson, R.M.C., Irvine, R.F., Bray, J., and Quinn, P.J. (1984)Biochem. Biophys. Res. Commun. 125, 836–842.

    Article  PubMed  CAS  Google Scholar 

  58. Reinhold, S.L., Zimmerman, G.A., Prescott, S.M., and McIntyre, T.M. (1989)J. Biol. Chem. 264, 21652–21659.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institut National de la Santé et de la Recherche Médical U200, 92140, Clamart, France

    Ewa Ninio & Francine Joly

Authors
  1. Ewa Ninio
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Francine Joly
    View author publications

    You can also search for this author in PubMed Google Scholar

About this article

Cite this article

Ninio, E., Joly, F. Transmembrane signalling and paf-acether biosynthesis. Lipids 26, 1034–1037 (1991). https://doi.org/10.1007/BF02536497

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02536497

Keywords

Search

Navigation